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Database: UniProt
Entry: A0A3Q2UVH5_HAPBU
LinkDB: A0A3Q2UVH5_HAPBU
Original site: A0A3Q2UVH5_HAPBU 
ID   A0A3Q2UVH5_HAPBU        Unreviewed;       633 AA.
AC   A0A3Q2UVH5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   Name=DDX5 {ECO:0000313|Ensembl:ENSHBUP00000001694.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000001694.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000001694.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC       {ECO:0000256|RuleBase:RU000492}.
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DR   RefSeq; XP_005934556.1; XM_005934494.1.
DR   AlphaFoldDB; A0A3Q2UVH5; -.
DR   STRING; 8153.ENSHBUP00000001694; -.
DR   Ensembl; ENSHBUT00000013361.1; ENSHBUP00000001694.1; ENSHBUG00000002856.1.
DR   GeneID; 102308726; -.
DR   GeneTree; ENSGT00940000154705; -.
DR   OMA; TRVPSIM; -.
DR   OrthoDB; 5477821at2759; -.
DR   Proteomes; UP000264840; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   CDD; cd18787; SF2_C_DEAD; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1.
DR   PANTHER; PTHR47958:SF90; ATP-DEPENDENT RNA HELICASE DDX5-RELATED; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000492};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU000492};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000492};
KW   Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000492}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264840}.
FT   DOMAIN          98..126
FT                   /note="DEAD-box RNA helicase Q"
FT                   /evidence="ECO:0000259|PROSITE:PS51195"
FT   DOMAIN          129..304
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          332..479
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           98..126
FT                   /note="Q motif"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..503
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..633
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   633 AA;  70421 MW;  EFCDA5CD04A67823 CRC64;
     MPGFSDRDRG RDRGYGGGPP RFGGGGGGNR GGPPPGKFGN PGERLRKKHW NLDELPKFQK
     NFYQEHPDVT RRPLQEVEQY RRSKEVTVKG RDCPKPIVKF HEAAFPSYVM DVIVKQNWTE
     PTPIQSQGWP VALSGKDMVG IAQTGSGKTL AYLLPAIVHI QHQPFLEHGD GPICLVLAPT
     RELAQQVQQV AAEYGRASRL KSTCIYGGAP KGPQIRDLER GVEICIATPG RLIDFLECGK
     TNLRRCTYLV LDEADRMLDM GFEPQIRKIV DQIRPDRQTL MWSATWPKEV RQLAEDFLKD
     YVQINIGALQ LSANHNILQI VDVCNDLEKE DKLIRLLEEI MSEKENKTII FVETKRRCDE
     LTRRMRRDGW PAMGIHGDKS QQERDWVLNE FRYGKAPILI ATDVASRGLD VEDVKFVINY
     DYPNSSEDYI HRIGRTARSQ KTGTAYTFFT PNNMKQASDL ISVLREANQA INPKLIQMAE
     DRGGRGRGGR GGYKDDRRDR YSGGGRSNFS GSSYRDSDRG FGSGPKSSFG GSKAQNGGNY
     GGNSGNSSGN YGSSNYSNSN GQGNFGAPTN QVGGFGNQSF QGPPQFGGMQ RATQNGMNHP
     PFPFNSQPPP PQAQQQPPPP PMVPYTMPPP FPQ
//
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